BIOL 1411: CHAPTER 3
35 Cards in this Set
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what are the 4 molecules that characterize living things
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protein
carbohydrates
lipids
nucleic acids
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polymers
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large molecules made up of monomers which are covalently bonded
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monomers
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what make up polymers
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what are proteins made up of
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20 amino acids
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what is nucleic acid formed from
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nucleotides
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macromolecules
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polymers with molecular weights exceeding 1,000
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functional groups
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small groups of atoms
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isomers
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molecules with same chemical formula, same kind & number of atoms but different arrangements
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structural isomers
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differ on how atoms are joined together
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cis-trans isomers
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double bond between 2 carbon atoms
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optical isomers
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carbon atom had 4 different atoms or groups of atoms attached to it
2 different ways of making attachment, mirror-optical
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condensation reactions
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dehydration reactions; loss of water, how polymers formed from monomers
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hydrolysis reaction
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opposite reaction, breakdown of polymers into monomers
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enzymes
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catalyze (speed up) biochemical reactions
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structural proteins
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provide physical stability and movement
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defence proteins
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recognize and respond to nonself substances (antibodies)
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signaling proteins
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control physiology process (hormones)
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receptor proteins
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receive and respond to chemical reactions
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membrane transporters
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regulate passage of substances across cellular membranes
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storage proteins
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store amino acids for later use
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transport proteins
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bind & carry substances within the organism
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proteins
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polymers made of 20 amino acids in different orders
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polypeptide chains
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unbranched (linear) polymers of covalently linked amino acids
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amino acid
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corboxyl functional group & amino functional group attached to same carbon atom
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what makes up an amino acid
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amino group
α carbon
hydrogen atom
carboxyl group
side chain (R group)
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disulfide bridge
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determines how polypeptide chain folds (S-S)
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peptide linkage (peptide bond)
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bond between amino acids in a protein; formed between carboxyl group and amino group
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primary structure of protein
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the sequence of amino acids in a polypeptide chain
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secondary structure of protein
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repeated spacial patterns in different regions of polypeptide chain
α (alpha) helix
β (beta) pleated sheet
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α (alpha) helix
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right-handed coil
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β (beta) pleated sheet
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formed from 2 or more polypeptide chains
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tertiary structure
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when polypeptide chain is bent at specific sites and then folded back and forth
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denatured
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loss of activity of an enzyme or nucleic acid molecule
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quaternary structure
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the ways the polypeptides bind together and interact
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chaperones
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class of proteins that protect 3D shape
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BIOL 1411: Chapter 3